The body's immune system is an effective weapon against disease, and immunotherapy of cancer cell research
is the current frontier in the treatment of cancer and other diseases.
Recently, researchers at Notre Dame University have identified specific features of the reaction of two distinct peptide antigens to a T-cell receptor (TCR), which provides new clues to optimizing molecular structure for the development of immunotherapy of cancer cell research.
The results were published in the latest issue of Nature Chemical Biology.
"We found that T-cell receptors might be more cross-reactive than we thought they were." Said the lead author Timothy Riley, a former graduate student assistant at Baker and now co-founder, scientist and director of the startup Structured Immunity, which incubated through Notre Dame's IDEA center to reduce the risk of early exposure of immunotherapy.
T cells, a subtype of white blood cells, are responsible for sensing whether the body is healthy or infected, but they often ignore the presence of cancer cells in the body. In T-cell immunotherapy, cancer cells are allowed to look for and destroy specific cells by adding receptor molecules that are recognized by the body's immune system. Although this treatment is effective in some cases, it often affects healthy cells. Therefore, researchers hope to predict responsiveness and reduce nonspecific responses as far as possible.
In this study, the authors found that a TCR molecule called DMF5 binds to a variety of different peptides. Two different peptide antigens, which bind to DMF5, have the same effect in stimulating receptors and inducing immune responses. "As long as it happens, its working style is not important," the author said.
In summary, although previous studies have known that TCR can attack healthy cells, this study fully explains why.